title: Angiotensin-I converting enzyme (ACE) inhibitory mechanism of tripeptides containing aromatic residues.
abstract: Angiotensin-I converting enzyme (ACE) plays important roles in the regulation of blood pressure, and ACE inhibitory peptides in food materials have attracted attention for their antihypertensive function. In this study, the function of amino acids in ACE inhibitory tripeptides was clarified.
authors.affiliation: Department of Chemical Science and Engineering, Graduate School of Engineering, Kobe University, 1-1 Rokkodai, Nada, Kobe 657-8501, Japan.
authors.forename: Yuka
authors.initials: Y
authors.lastname: Kobayashi
authors.forename: Tadashi
authors.initials: T
authors.lastname: Yamauchi
authors.forename: Tomohisa
authors.initials: T
authors.lastname: Katsuda
authors.forename: Hideki
authors.initials: H
authors.lastname: Yamaji
authors.forename: Shigeo
authors.initials: S
authors.lastname: Katoh
mesh_terms: D000596:Amino Acids / Q000737:chemistry*; D000806:Angiotensin-Converting Enzyme Inhibitors / Q000737:chemistry*; D003198:Computer Simulation; D004791:Enzyme Inhibitors / Q000737:chemistry; D006841:Hydrocarbons, Aromatic / Q000737:chemistry*; D008956:Models, Chemical; D010455:Peptides / Q000737:chemistry*
chemical_list: D000596:Amino Acids; D000806:Angiotensin-Converting Enzyme Inhibitors; D004791:Enzyme Inhibitors; D006841:Hydrocarbons, Aromatic; D010455:Peptides